https://ogma.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:35792 Thu 28 Nov 2019 16:30:09 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:10871 5000 bp per second—and is powerful enough to remove other proteins from the DNA. In bacteria it is localised to the site of cell division, the septum, where it functions as a DNA pump at the late stages of the cell cycle, to expedite cytokinesis and chromosome segregation. The N terminus of the protein is involved in the cell-cycle-specific localisation and assembly of the cell-division machinery, whereas the C terminus forms the motor. The motor portion of FtsK has been studied by a combination of biochemistry, genetics, X-ray crystallography and single-molecule mechanical assays, and these will be the focus here. The motor can be divided into three subdomains: α, β and γ. The α and β domains multimerise to produce a hexameric ring with a central channel for dsDNA, and contain a RecA-like nucleotide-binding/hydrolysis fold. The motor is given directionality by the regulatory γ domain, which binds to polarised chromosomal sequences—5′-GGGNAGGG-3′, known as KOPS—to ensure that the motor is loaded onto DNA in a specific orientation such that subsequent translocation is always towards the region of the chromosome where replication usually terminates (the terminus), and specifically to the 28 bp dif site, located in this region. Once the FtsK translocase has located the dif site it then interacts with the XerCD site-specific recombinases to activate recombination.]]> Sat 24 Mar 2018 08:14:31 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:10662 Sat 24 Mar 2018 08:12:42 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:18361 Sat 24 Mar 2018 07:52:40 AEDT ]]>